ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Beta-arrestin-1

Intramolecular
Cysteine 140 and cysteine 242
Cysteine 59 and cysteine 125
Cysteine 59 and cysteine 81
A redox-regulated disulphide may form within Beta-arrestin-1 between cysteines 140 and 242. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6kl7
Structure name
beta-arrestin 1 mutant s13d/t275d
Structure deposition date
2019-07-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P29066
Residue number A
140
Residue number B
242
Peptide name
Beta-arrestin-1

Ligandability

Cysteine 140 of Beta-arrestin-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 242 of Beta-arrestin-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Beta-arrestin-1 between cysteines 59 and 125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
7dfb
Structure name
crystal of arrestin2-v2rpp-6-7-fab30 complex
Structure deposition date
2020-11-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
96
Peptide accession
P17870
Residue number A
59
Residue number B
125
Peptide name
Beta-arrestin-1

Ligandability

Cysteine 59 of Beta-arrestin-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 125 of Beta-arrestin-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Beta-arrestin-1 between cysteines 59 and 81.

Details

Redox score ?
nan
PDB code
6pwc
Structure name
a complex structure of arrestin-2 bound to neurotensin receptor 1
Structure deposition date
2019-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
12
Peptide accession
P49407
Residue number A
59
Residue number B
81
Peptide name
Beta-arrestin-1

Ligandability

Cysteine 59 of Beta-arrestin-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 81 of Beta-arrestin-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 81 in protein B could not be asigned to a Uniprot residue.
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